STRINGSTRING
STY0269 STY0269 STY1778 STY1778 STY2654 STY2654 STY2767 STY2767 trpS trpS STY3196 STY3196 STY2948 STY2948 STY0541 STY0541 STY0585 STY0585 STY0699 STY0699 STY0724 STY0724 STY0961 STY0961 asnS asnS STY1673 STY1673 STY0055 STY0055 valS valS
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
STY0269prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] (572 aa)
STY1778threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). (642 aa)
STY2654glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). (474 aa)
STY2767Similar to Salmonella typhimurium histidyl-tRNA synthetase SW:SYH_SALTY (O52765) (423 aa) fasta scores: E(): 0, 99.3% id in 423 aa; Orthologue of E. coli hisS (SYH_ECOLI); Fasta hit to SYH_ECOLI (423 aa), 95% identity in 423 aa overlap. (424 aa)
trpStryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (334 aa)
STY3196Lysyl tRNA synthetase (LysRS); Fasta hit to SYK2_ECOLI (504 aa), 90% identity in 504 aa overlap; Orthologue of E. coli lysS (SYK1_ECOLI); Fasta hit to SYK1_ECOLI (504 aa), 95% identity in 504 aa overlap; Belongs to the class-II aminoacyl-tRNA synthetase family. (505 aa)
STY2948alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain; Belongs to the class-II aminoacyl-tRNA synthetase family. (876 aa)
STY0541Conserved hypothetical protein; Orthologue of E. coli YBAK_ECOLI; Fasta hit to YBAK_ECOLI (159 aa), 91% identity in 159 aa overlap; Belongs to the prolyl-tRNA editing family. YbaK/EbsC subfamily. (159 aa)
STY0585cysteinyl-tRNA synthetase; Orthologue of E. coli cysS (SYC_ECOLI); Fasta hit to SYC_ECOLI (461 aa), 94% identity in 461 aa overlap; Belongs to the class-I aminoacyl-tRNA synthetase family. (461 aa)
STY0699leucyl-tRNA synthetase; Orthologue of E. coli leuS (SYL_ECOLI); Fasta hit to SYL_ECOLI (860 aa), 95% identity in 860 aa overlap; Belongs to the class-I aminoacyl-tRNA synthetase family. (860 aa)
STY0724glutaminyl-tRNA synthetase; Orthologue of E. coli glnS (SYQ_ECOLI); Fasta hit to SYQ_ECOLI (553 aa), 96% identity in 554 aa overlap. (555 aa)
STY0961seryl-tRNA synthetase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). (430 aa)
asnSSimilar to Escherichia coli asparaginyl-tRNA synthetase SW:SYN_ECOLI (P17242) fasta scores: E(): 0, 94.6% id in 465 aa. (466 aa)
STY1673tyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily. (424 aa)
STY0055isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily. (944 aa)
valSvalyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. (951 aa)
Your Current Organism:
Salmonella enterica Typhi
NCBI taxonomy Id: 220341
Other names: S. enterica subsp. enterica serovar Typhi str. CT18, Salmonella enterica subsp. enterica serovar Typhi CT18, Salmonella enterica subsp. enterica serovar Typhi str. CT18, Salmonella enterica subsp. enterica serovar Typhi strain CT18, Salmonella typhi CT18
Server load: low (18%) [HD]